Anti-ILK2/ILK1

In 1X PBS, pH 7.4, with 0.09% sodium azide. Transduction of extracellular matrix signals through integrins influences intracellular and extracellular functions, and appears to require interaction of integrin cytoplasmic domains with cellular proteins. Integrin-linked kinase (ILK) is an ankyrin repeat containing 51 kDa receptor-proximate serine-threonine kinase (1), with a reported migration rate of 59K. This 451 amino acid protein interacts with the cytoplasmic domain of the beta-1 integrin subunit and contains sequence motifs found in pleckstrin homology domains capable of interacting with phosphoinositide lipids. ILK is an upstream regulator of Pi(3)K dependant activation of protein kinase B (PKB/AKT) and inhibition of glycogen synthase kinase 3 (GSK-3). ILK2 expression is associated with mediation of cell architecture, adhesion to integrin substrates and anchorage-dependent growth in epithelial cells. ILK2 is overexpressed in some highly invasive tumor cell lines. Protein function: Receptor-proximal protein kinase regulating integrin- mediated signal transduction. May act as a mediator of inside-out integrin signaling. Focal adhesion protein part of the complex ILK-PINCH. This complex is considered to be one of the convergence points of integrin- and growth factor-signaling pathway. Could be implicated in mediating cell architecture, adhesion to integrin substrates and anchorage-dependent growth in epithelial cells. Phosphorylates beta-1 and beta-3 integrin subunit on serine and threonine residues, but also AKT1 and GSK3B. [The UniProt Consortium]